URE2/YNL229C Literature Guide Help

Other names published for URE2: [URE3], YNL229C

URE2 - Fungal Related Genes/Proteins (22)

ReferenceOther Genes Addressed
Kelly AC, et al.  (2012) Sex, prions, and plasmids in yeast. Proc Natl Acad Sci U S A 109(40):E2683-90
Edskes HK, et al.  (2011) Prion-forming ability of ure2 of yeasts is not evolutionarily conserved. Genetics 188(1):81-90
Engel A, et al.  (2011) Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel ?-sheet structure. Biochemistry 50(27):5971-8
Wang YQ, et al.  (2011) Relationship between Prion Propensity and the Rates of Individual Molecular Steps of Fibril Assembly. J Biol Chem 286(14):12101-7
Wang YQ, et al.  (2011) The fibrils of Ure2p homologs from Saccharomyces cerevisiae and Saccharoymyces paradoxus have similar cross-? structure in both dried and hydrated forms. J Struct Biol 174(3):505-11
Crapeau M, et al.  (2009) The cellular concentration of the yeast ure2p prion protein affects its propagation as a prion. Mol Biol Cell 20(8):2286-96
Edskes HK, et al.  (2009) Prion variants and species barriers among Saccharomyces ure2 proteins. Genetics 181(3):1159-67
Reineke LC and Merrick WC  (2009) Characterization of the functional role of nucleotides within the URE2 IRES element and the requirements for eIF2A-mediated repression. RNA 15(12):2264-77
Harrison LB, et al.  (2007) Evolution of Budding Yeast Prion-determinant Sequences Across Diverse Fungi. J Mol Biol 368(1):273-82
Immel F, et al.  (2007) In Vitro Analysis of SpUre2p, a Prion-related Protein, Exemplifies the Relationship between Amyloid and Prion. J Biol Chem 282(11):7912-20
McGoldrick S, et al.  (2005) Glutathione transferase-like proteins encoded in genomes of yeasts and fungi: insights into evolution of a multifunctional protein superfamily. FEMS Microbiol Lett 242(1):1-12
Talarek N, et al.  (2005) The [URE3] prion is not conserved among Saccharomyces species. Genetics 171(1):23-34
Baxa U, et al.  (2004) Prions of Saccharomyces and Podospora. Contrib Microbiol 11():50-71
Baudin-Baillieu A, et al.  (2003) Conservation of the prion properties of Ure2p through evolution. Mol Biol Cell 14(8):3449-58
Harrison PM and Gerstein M  (2003) A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes. Genome Biol 4(6):R40
Edskes HK and Wickner RB  (2002) Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein. Proc Natl Acad Sci U S A 99 Suppl 4:16384-91
Fraser JA, et al.  (2002) A gene from Aspergillus nidulans with similarity to URE2 of Saccharomyces cerevisiae encodes a glutathione S-transferase which contributes to heavy metal and xenobiotic resistance. Appl Environ Microbiol 68(6):2802-8
Choi JH, et al.  (1998) A novel membrane-bound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae. J Biol Chem 273(45):29915-22
Lorenz MC and Heitman J  (1998) Regulators of pseudohyphal differentiation in Saccharomyces cerevisiae identified through multicopy suppressor analysis in ammonium permease mutant strains. Genetics 150(4):1443-57
Coffman JA, et al.  (1996) Gat1p, a GATA family protein whose production is sensitive to nitrogen catabolite repression, participates in transcriptional activation of nitrogen-catabolic genes in Saccharomyces cerevisiae. Mol Cell Biol 16(3):847-58
Derkatch IL, et al.  (1996) Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144(4):1375-86
Coschigano PW and Magasanik B  (1991) The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol Cell Biol 11(2):822-32